Characterization of a conserved "threonine clasp" in CAP-Gly domains: role of a functionally critical OH/pi interaction in protein recognition.
XH/pi hydrogen bonds have been predicted to make important contributions to protein structure and function. NMR evidence is presented for an OH/pi interaction between a highly conserved threonine and phenylalanine pair found specifically in CAP-Gly domains associated with mictrotubule plus ends. The functional contribution of this nonclassical hydrogen bond in target peptide recognition is demonstrated via subtle point mutagenesis. The OH/pi interaction is part of a TxFxxxxW motif that comprises a conserved "threonine clasp" that defines function in CAP-Gly domains.
Plevin
Michael J
MJ
Division of Signaling Biology, Ontario Cancer Institute, University of Toronto, 101 College Street, Toronto, Ontario, M5G 1L7, Canada. michael.plevin@ibs.fr
Hayashi
Ikuko
I
Ikura
Mitsuhiko
M
D000072159:Dynactin Complex; D006801:Humans; D006860:Hydrogen Bonding; D008869:Microtubule-Associated Proteins / Q000737:chemistry*; D008958:Models, Molecular; D009363:Neoplasm Proteins / Q000737:chemistry*; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010446:Peptide Fragments / Q000737:chemistry; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D013912:Threonine / Q000737:chemistry*
D000072159:Dynactin Complex; D008869:Microtubule-Associated Proteins; D009363:Neoplasm Proteins; D010446:Peptide Fragments; C076744:cytoplasmic linker protein 170; D013912:Threonine